Identification of three annexin ix isoforms generated by alternative splicing of the carboxyl-terminal exon in silkworm, bombyx mori

Qing You Xia, Hiroshi Fujii, Takahiro Kusakabe, Yutaka Banno

研究成果: ジャーナルへの寄稿記事

5 引用 (Scopus)

抄録

Annexins (ANXs) are a family of structurally related proteins with Ca2--dependent phospholipid- binding properties. Here we report the cloning of three cDNAs each encoding annexin IX (ANX IX) isoforms from unfertilized eggs of the silkworm, Bombyx mori. The analysis of exon/intron structures showed that the three mRNAs, named ANX IX-A (2300 bp), ANX IX-B (1884 bp) and ANX IX-C (1409 bp), respectively, were generated from a single gene by alternative usage of a 3′-splice site of the last exon. Thus the three isoforms have an identical sequence from amino acid residues 1 to 307 and this region shows approximately 77% identity to Drosophila melanogaster ANX IX. Only amino acid residues 308-324 (A) or 308-323 (B and C), which correspond to the C-terminal tail, are different in the three proteins. A RT-PCR analysis indicated that the three isoforms of silkworm ANX IX were specifically expressed in various larval tissues and development stages. Interestingly, the C-terminal tail in ANXs I, II and V were previously confirmed as a binding region for protein kinase C. Thus generation of the three ANX IX isoforms in the silkworm, that are different from other ANXs, may have a functional significance other than binding to Ca2+.

元の言語英語
ページ(範囲)9-14
ページ数6
ジャーナルInsect Biochemistry and Molecular Biology
32
発行部数1
DOI
出版物ステータス出版済み - 1 1 2001

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Annexins
Bombyx
alternative splicing
Alternative Splicing
Bombyx mori
silkworms
exons
Exons
Protein Isoforms
tail
calcium
amino acids
binding properties
protein kinase C
Drosophila melanogaster
introns
molecular cloning
phospholipids
proteins
reverse transcriptase polymerase chain reaction

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Insect Science

これを引用

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abstract = "Annexins (ANXs) are a family of structurally related proteins with Ca2--dependent phospholipid- binding properties. Here we report the cloning of three cDNAs each encoding annexin IX (ANX IX) isoforms from unfertilized eggs of the silkworm, Bombyx mori. The analysis of exon/intron structures showed that the three mRNAs, named ANX IX-A (2300 bp), ANX IX-B (1884 bp) and ANX IX-C (1409 bp), respectively, were generated from a single gene by alternative usage of a 3′-splice site of the last exon. Thus the three isoforms have an identical sequence from amino acid residues 1 to 307 and this region shows approximately 77{\%} identity to Drosophila melanogaster ANX IX. Only amino acid residues 308-324 (A) or 308-323 (B and C), which correspond to the C-terminal tail, are different in the three proteins. A RT-PCR analysis indicated that the three isoforms of silkworm ANX IX were specifically expressed in various larval tissues and development stages. Interestingly, the C-terminal tail in ANXs I, II and V were previously confirmed as a binding region for protein kinase C. Thus generation of the three ANX IX isoforms in the silkworm, that are different from other ANXs, may have a functional significance other than binding to Ca2+.",
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T1 - Identification of three annexin ix isoforms generated by alternative splicing of the carboxyl-terminal exon in silkworm, bombyx mori

AU - Xia, Qing You

AU - Fujii, Hiroshi

AU - Kusakabe, Takahiro

AU - Banno, Yutaka

PY - 2001/1/1

Y1 - 2001/1/1

N2 - Annexins (ANXs) are a family of structurally related proteins with Ca2--dependent phospholipid- binding properties. Here we report the cloning of three cDNAs each encoding annexin IX (ANX IX) isoforms from unfertilized eggs of the silkworm, Bombyx mori. The analysis of exon/intron structures showed that the three mRNAs, named ANX IX-A (2300 bp), ANX IX-B (1884 bp) and ANX IX-C (1409 bp), respectively, were generated from a single gene by alternative usage of a 3′-splice site of the last exon. Thus the three isoforms have an identical sequence from amino acid residues 1 to 307 and this region shows approximately 77% identity to Drosophila melanogaster ANX IX. Only amino acid residues 308-324 (A) or 308-323 (B and C), which correspond to the C-terminal tail, are different in the three proteins. A RT-PCR analysis indicated that the three isoforms of silkworm ANX IX were specifically expressed in various larval tissues and development stages. Interestingly, the C-terminal tail in ANXs I, II and V were previously confirmed as a binding region for protein kinase C. Thus generation of the three ANX IX isoforms in the silkworm, that are different from other ANXs, may have a functional significance other than binding to Ca2+.

AB - Annexins (ANXs) are a family of structurally related proteins with Ca2--dependent phospholipid- binding properties. Here we report the cloning of three cDNAs each encoding annexin IX (ANX IX) isoforms from unfertilized eggs of the silkworm, Bombyx mori. The analysis of exon/intron structures showed that the three mRNAs, named ANX IX-A (2300 bp), ANX IX-B (1884 bp) and ANX IX-C (1409 bp), respectively, were generated from a single gene by alternative usage of a 3′-splice site of the last exon. Thus the three isoforms have an identical sequence from amino acid residues 1 to 307 and this region shows approximately 77% identity to Drosophila melanogaster ANX IX. Only amino acid residues 308-324 (A) or 308-323 (B and C), which correspond to the C-terminal tail, are different in the three proteins. A RT-PCR analysis indicated that the three isoforms of silkworm ANX IX were specifically expressed in various larval tissues and development stages. Interestingly, the C-terminal tail in ANXs I, II and V were previously confirmed as a binding region for protein kinase C. Thus generation of the three ANX IX isoforms in the silkworm, that are different from other ANXs, may have a functional significance other than binding to Ca2+.

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